Armadillo motifs involved in vesicular transport

PLoS One. 2010 Feb 1;5(2):e8991. doi: 10.1371/journal.pone.0008991.

Abstract

Armadillo (ARM) repeat proteins function in various cellular processes including vesicular transport and membrane tethering. They contain an imperfect repeating sequence motif that forms a conserved three-dimensional structure. Recently, structural and functional insight into tethering mediated by the ARM-repeat protein p115 has been provided. Here we describe the p115 ARM-motifs for reasons of clarity and nomenclature and show that both sequence and structure are highly conserved among ARM-repeat proteins. We argue that there is no need to invoke repeat types other than ARM repeats for a proper description of the structure of the p115 globular head region. Additionally, we propose to define a new subfamily of ARM-like proteins and show lack of evidence that the ARM motifs found in p115 are present in other long coiled-coil tethering factors of the golgin family.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Motifs*
  • Amino Acid Sequence
  • Armadillo Domain Proteins / chemistry
  • Armadillo Domain Proteins / genetics
  • Armadillo Domain Proteins / physiology*
  • Biological Transport
  • Crystallography, X-Ray
  • Golgi Matrix Proteins
  • Humans
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Multimerization
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Repetitive Sequences, Amino Acid
  • Sequence Homology, Amino Acid
  • Transport Vesicles / metabolism*
  • Vesicular Transport Proteins / chemistry
  • Vesicular Transport Proteins / genetics
  • Vesicular Transport Proteins / physiology*

Substances

  • Armadillo Domain Proteins
  • Golgi Matrix Proteins
  • Vesicular Transport Proteins
  • vesicular transport factor p115